A new era for understanding amyloid structures and disease
MG Iadanza, MP Jackson, EW Hewitt… - … reviews Molecular cell …, 2018 - nature.com
The aggregation of proteins into amyloid fibrils and their deposition into plaques and
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …
[HTML][HTML] α-Synuclein misfolding and Parkinson's disease
Substantial evidence links α-synuclein, a small highly conserved presynaptic protein with
unknown function, to both familial and sporadic Parkinson's disease (PD). α-Synuclein has …
unknown function, to both familial and sporadic Parkinson's disease (PD). α-Synuclein has …
[HTML][HTML] Focus: the aging brain: amyloid-beta Alzheimer targets—protein processing, lipid rafts, and amyloid-beta pores
M LaFontaine, M Cumbay - The Yale journal of biology and …, 2016 - ncbi.nlm.nih.gov
Amyloid beta (Aβ), the hallmark of Alzheimer's Disease (AD), now appears to be deleterious
in its low number aggregate form as opposed to the macroscopic Aβ fibers historically seen …
in its low number aggregate form as opposed to the macroscopic Aβ fibers historically seen …
Internalisation and toxicity of amyloid‐β 1‐42 are influenced by its conformation and assembly state rather than size
Amyloid fibrils found in plaques in Alzheimer's disease (AD) brains are composed of amyloid‐
β peptides. Oligomeric amyloid‐β 1‐42 (Aβ42) is thought to play a critical role in …
β peptides. Oligomeric amyloid‐β 1‐42 (Aβ42) is thought to play a critical role in …
Cell damage in light chain amyloidosis: fibril internalization, toxicity and cell-mediated seeding
Light chain (AL) amyloidosis is an incurable human disease characterized by the misfolding,
aggregation, and systemic deposition of amyloid composed of immunoglobulin light chains …
aggregation, and systemic deposition of amyloid composed of immunoglobulin light chains …
Inhibition of insulin amyloid fibrillation by a novel amphipathic heptapeptide
The aggregation of insulin into amyloid fibers has been a limiting factor in the development
of fast acting insulin analogues, creating a demand for excipients that limit aggregation …
of fast acting insulin analogues, creating a demand for excipients that limit aggregation …
High intrinsic mechanical flexibility of mouse prion nanofibrils revealed by measurements of axial and radial Young's moduli
Self-templated protein aggregation and intracerebral deposition of aggregates, sometimes
in the form of amyloid fibrils, is a hallmark of mammalian prion diseases. What distinguishes …
in the form of amyloid fibrils, is a hallmark of mammalian prion diseases. What distinguishes …
Nonspecific prion protein–nucleic acid interactions lead to different aggregates and cytotoxic species
B Macedo, TA Millen, CACA Braga, MPB Gomes… - Biochemistry, 2012 - ACS Publications
A misfolded form of the prion protein (PrP) is the primary culprit in mammalian prion
diseases. It has been shown that nucleic acids catalyze the misfolding of cellular PrP into a …
diseases. It has been shown that nucleic acids catalyze the misfolding of cellular PrP into a …
Strain-dependent profile of misfolded prion protein aggregates
R Morales, PP Hu, C Duran-Aniotz, F Moda… - Scientific Reports, 2016 - nature.com
Prions are composed of the misfolded prion protein (PrPSc) organized in a variety of
aggregates. An important question in the prion field has been to determine the identity of …
aggregates. An important question in the prion field has been to determine the identity of …
Development of the structural core and of conformational heterogeneity during the conversion of oligomers of the mouse prion protein to worm-like amyloid fibrils
Understanding how structure develops during the course of amyloid fibril formation by the
prion protein is important for understanding prion diseases. Determining how conformational …
prion protein is important for understanding prion diseases. Determining how conformational …